M3K18_ARATH
ID M3K18_ARATH Reviewed; 339 AA.
AC Q9ZVP5;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 18 {ECO:0000303|PubMed:26443375};
DE EC=2.7.11.25 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:25680457, ECO:0000269|PubMed:26443375};
GN Name=MAPKKK18 {ECO:0000303|PubMed:26443375};
GN Synonyms=MAP3K18 {ECO:0000303|PubMed:25720833};
GN OrderedLocusNames=At1g05100 {ECO:0000312|Araport:AT1G05100};
GN ORFNames=T7A14.2 {ECO:0000312|EMBL:AAC97990.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-32 AND THR-161,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, INTERACTION
RP WITH ABI1, REGULATION BY THE PROTEASOME, INDUCTION BY ABSCISIC ACID,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=26443375; DOI=10.1093/pcp/pcv146;
RA Mitula F., Tajdel M., Ciesla A., Kasprowicz-Maluski A., Kulik A.,
RA Babula-Skowronska D., Michalak M., Dobrowolska G., Sadowski J.,
RA Ludwikow A.;
RT "Arabidopsis ABA-activated kinase MAPKKK18 is regulated by protein
RT phosphatase 2C ABI1 and the ubiquitin-proteasome pathway.";
RL Plant Cell Physiol. 56:2351-2367(2015).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY ABSCISIC ACID AND OSMOTIC
RP STRESSES, AND INTERACTION WITH MKK3.
RC STRAIN=cv. Columbia;
RX PubMed=25720833; DOI=10.1111/tpj.12808;
RA Danquah A., de Zelicourt A., Boudsocq M., Neubauer J., Frei Dit Frey N.,
RA Leonhardt N., Pateyron S., Gwinner F., Tamby J.P., Ortiz-Masia D.,
RA Marcote M.J., Hirt H., Colcombet J.;
RT "Identification and characterization of an ABA-activated MAP kinase cascade
RT in Arabidopsis thaliana.";
RL Plant J. 82:232-244(2015).
RN [6]
RP FUNCTION, MUTAGENESIS OF LYS-32, INDUCTION BY ABSCISIC ACID, INTERACTION
RP WITH MKK3, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP AUTOPHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=25680457; DOI=10.1007/s11103-015-0295-0;
RA Matsuoka D., Yasufuku T., Furuya T., Nanmori T.;
RT "An abscisic acid inducible Arabidopsis MAPKKK, MAPKKK18 regulates leaf
RT senescence via its kinase activity.";
RL Plant Mol. Biol. 87:565-575(2015).
RN [7]
RP INTERACTION WITH SRK2E, AND SUBCELLULAR LOCATION.
RX PubMed=26852793; DOI=10.1080/15592324.2016.1139277;
RA Tajdel M., Mitula F., Ludwikow A.;
RT "Regulation of Arabidopsis MAPKKK18 by ABI1 and SnRK2, components of the
RT ABA signaling pathway.";
RL Plant Signal. Behav. 11:E1139277-E1139277(2016).
RN [8]
RP REVIEW ON MITOGEN-ACTIVATED PROTEIN KINASE CASCADES.
RX PubMed=30349547; DOI=10.3389/fpls.2018.01387;
RA Jagodzik P., Tajdel-Zielinska M., Ciesla A., Marczak M., Ludwikow A.;
RT "Mitogen-activated protein kinase cascades in plant hormone signaling.";
RL Front. Plant Sci. 9:1387-1387(2018).
CC -!- FUNCTION: Component of the abscisic acid (ABA) signaling pathway that
CC acts as ABA signal transducer in the context of abiotic stresses
CC (PubMed:26443375, PubMed:25720833, PubMed:25680457). Triggers MPK1,
CC MPK2, MPK7 and MPK14 activation in a MKK3-dependent manner and MPK6
CC activation in a MKK3-independent manner. Mediates the ABA-dependent
CC activation of the MKK3-MPK7 module (PubMed:25720833). Positive
CC regulator of ABA responses leading to the induction of gene expression
CC (e.g. RD29B and RAB18) and involved in various responses including
CC stomatal development, stomatal movement, inhibition of germination and
CC root growth (PubMed:26443375). Promotes leaf senescence
CC (PubMed:25680457). {ECO:0000269|PubMed:25680457,
CC ECO:0000269|PubMed:25720833, ECO:0000269|PubMed:26443375}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00159,
CC ECO:0000269|PubMed:25680457, ECO:0000269|PubMed:26443375};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.25; Evidence={ECO:0000255|PROSITE-ProRule:PRU00159,
CC ECO:0000269|PubMed:25680457, ECO:0000269|PubMed:26443375};
CC -!- ACTIVITY REGULATION: Kinase activity is activated by abscisic acid
CC (ABA) (PubMed:26443375, PubMed:25680457). Inhibited by ABI1. Activated
CC by SRK2E (PubMed:26443375). {ECO:0000269|PubMed:25680457,
CC ECO:0000269|PubMed:26443375}.
CC -!- SUBUNIT: Interacts with ABI1 (PubMed:26443375). Binds to MKK3
CC (PubMed:25720833, PubMed:25680457). Associates with SRK2E within the
CC nucleus (PubMed:26852793). {ECO:0000269|PubMed:25680457,
CC ECO:0000269|PubMed:25720833, ECO:0000269|PubMed:26443375,
CC ECO:0000269|PubMed:26852793}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26443375,
CC ECO:0000269|PubMed:26852793}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers.
CC {ECO:0000269|PubMed:26443375}.
CC -!- DEVELOPMENTAL STAGE: In developing flowers, observed in sepals, anther
CC filaments, ovaries and meristem tissues. Also expressed in root
CC meristem tissues and in areas of lateral root formation. In leaves,
CC detected in guard cells and trichomes. {ECO:0000269|PubMed:26443375}.
CC -!- INDUCTION: Strongly induced by abscisic acid (ABA) in the flowers,
CC leaves and root tissues (PubMed:26443375, PubMed:25720833). Accumulates
CC in response to osmotic stresses (e.g. mannitol and NaCl)
CC (PubMed:25720833). {ECO:0000269|PubMed:25720833,
CC ECO:0000269|PubMed:26443375}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:25680457}.
CC -!- PTM: Unstable protein degraded by the proteasome pathway; this
CC degradation is promoted by ABI1, but blocked by ABA.
CC {ECO:0000269|PubMed:26443375}.
CC -!- DISRUPTION PHENOTYPE: More vigorous root growth, decreased abaxial
CC stomatal index and increased stomatal aperture. Reduced induction of
CC RD29B and RAB18 expression in response to treatment with abscisic acid
CC (ABA) (PubMed:26443375). In the double mutant map3k17 map3k18, impaired
CC MPK7 activation mediated by ABA (PubMed:25720833).
CC {ECO:0000269|PubMed:25720833, ECO:0000269|PubMed:26443375}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC005322; AAC97990.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27791.1; -; Genomic_DNA.
DR EMBL; AY064039; AAL36395.1; -; mRNA.
DR EMBL; AY091011; AAM14033.1; -; mRNA.
DR EMBL; BT004419; AAO42413.1; -; mRNA.
DR PIR; C86185; C86185.
DR RefSeq; NP_172003.1; NM_100389.4.
DR AlphaFoldDB; Q9ZVP5; -.
DR SMR; Q9ZVP5; -.
DR STRING; 3702.AT1G05100.1; -.
DR PaxDb; Q9ZVP5; -.
DR PRIDE; Q9ZVP5; -.
DR ProteomicsDB; 238649; -.
DR EnsemblPlants; AT1G05100.1; AT1G05100.1; AT1G05100.
DR GeneID; 839324; -.
DR Gramene; AT1G05100.1; AT1G05100.1; AT1G05100.
DR KEGG; ath:AT1G05100; -.
DR Araport; AT1G05100; -.
DR TAIR; locus:2205523; AT1G05100.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q9ZVP5; -.
DR OMA; ETWITVR; -.
DR OrthoDB; 801642at2759; -.
DR PhylomeDB; Q9ZVP5; -.
DR PRO; PR:Q9ZVP5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZVP5; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:1902457; P:negative regulation of stomatal opening; IMP:UniProtKB.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:1900057; P:positive regulation of leaf senescence; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:2000038; P:regulation of stomatal complex development; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IDA:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; ATP-binding; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..339
FT /note="Mitogen-activated protein kinase kinase kinase 18"
FT /id="PRO_0000440623"
FT DOMAIN 3..263
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 9..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O23304"
FT MUTAGEN 32
FT /note="K->M: Strongly reduced kinase activity and altered
FT subcellular localization outside the nucleus."
FT /evidence="ECO:0000269|PubMed:26443375"
FT MUTAGEN 32
FT /note="K->R: In KN; loss of kinase activity but enhanced
FT growth associated with larger leaves, higher weight,
FT increased chlorophyll contents and increased seed numbers.
FT Delayed leaves senescence."
FT /evidence="ECO:0000269|PubMed:25680457"
FT MUTAGEN 161
FT /note="T->E: Constitutively active kinase with normal
FT accumulation in the nucleus."
FT /evidence="ECO:0000269|PubMed:26443375"
SQ SEQUENCE 339 AA; 37742 MW; 552650D1E6B9DE17 CRC64;
MNWTRGKTLG RGSTATVSAA TCHESGETLA VKSAEFHRSE FLQREAKILS SLNSPYVIGY
RGCEITREPF HNNGEATTYS LLMEYAPYGT LTDVATKNGG FIDEARVVKY TRQILLGLEY
IHNSKGIAHC DIKGSNVLVG ENGEAKIADF GCAKWVEPEI TEPVRGTPAF MAPEAARGER
QGKESDIWAV GCTVIEMVTG SQPWIGADFT DPVSVLYRVG YLGELPELPC SLTEQAKDFL
GKCLKKEATE RWTASQLLNH PFLVNKEPEL VTGLVTNSPT SVTDQMFWRS VEEEVSEDRS
SWWECHEDER IGVLSWIGHV VVESTWDLDG EDWITVRRN
